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Sanzo Miyazawa
Sanzo Miyazawa
See: https://orcid.org/0000-0002-5063-3661
Verified email at sanzo.org - Homepage
Title
Cited by
Cited by
Year
Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation
S Miyazawa, RL Jernigan
Macromolecules 18 (3), 534-552, 1985
19801985
Residue–residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading
S Miyazawa, RL Jernigan
Journal of molecular biology 256 (3), 623-644, 1996
14651996
Two types of amino acid substitutions in protein evolution
T Miyata, S Miyazawa, T Yasunaga
Journal of molecular evolution 12, 219-236, 1979
5281979
Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the β-chain of major …
T Miyauchi, T Kanekura, A Yamaoka, M Ozawa, S Miyazawa, ...
The Journal of Biochemistry 107 (2), 316-323, 1990
2331990
Self‐consistent estimation of inter‐residue protein contact energies based on an equilibrium mixture approximation of residues
S Miyazawa, RL Jernigan
Proteins: Structure, Function, and Bioinformatics 34 (1), 49-68, 1999
2251999
Only DFL16, DSP2, and DQ52 gene families exist in mouse immunoglobulin heavy chain diversity gene loci, of which DFL16 and DSP2 originate from the same primordial DH gene
Y Ichihara, H Hayashida, S Miyazawa, Y Kurosawa
European journal of immunology 19 (10), 1849-1854, 1989
1521989
An empirical energy potential with a reference state for protein fold and sequence recognition
S Miyazawa, RL Jernigan
Proteins: Structure, Function, and Bioinformatics 36 (3), 357-369, 1999
1291999
A reliable sequence alignment method based on probabilities of residue correspondences
S Miyazawa
Protein Engineering, Design and Selection 8 (10), 999-1009, 1995
1231995
A new substitution matrix for protein sequence searches based on contact frequencies in protein structures
S Miyazawa, RL Jernigan
Protein Engineering, Design and Selection 6 (3), 267-278, 1993
1001993
Relationship between mutability, polarity and exteriority of amino acid residues in protein evolution
M GO, S MIYAZAWA
International journal of peptide and protein research 15 (3), 211-224, 1980
951980
How effective for fold recognition is a potential of mean force that includes relative orientations between contacting residues in proteins?
S Miyazawa, RL Jernigan
The Journal of chemical physics 122 (2), 2005
792005
Protein stability for single substitution mutants and the extent of local compactness in the denatured state
S Miyazawa, RL Jernigan
Protein Engineering, Design and Selection 7 (10), 1209-1220, 1994
751994
Evaluation of short‐range interactions as secondary structure energies for protein fold and sequence recognition
S Miyazawa, RL Jernigan
Proteins: Structure, Function, and Bioinformatics 36 (3), 347-356, 1999
491999
Equilibrium folding and unfolding pathways for a model protein
S Miyazawa, RL Jernigan
Biopolymers: Original Research on Biomolecules 21 (7), 1333-1363, 1982
371982
Identifying sequence–structure pairs undetected by sequence alignments
S Miyazawa, RL Jernigan
Protein Engineering 13 (7), 459-475, 2000
342000
Long‐and short‐range interactions in native protein structures are consistent/minimally frustrated in sequence space
S Miyazawa, RL Jernigan
Proteins: Structure, Function, and Bioinformatics 50 (1), 35-43, 2003
322003
Advantages of a mechanistic codon substitution model for evolutionary analysis of protein-coding sequences
S Miyazawa
PloS one 6 (12), e28892, 2011
212011
DNA Data Bank of Japan: Present Status and Future Plans
S Miyazawa
Computers and DNA: the proceedings of the Interface between Computation …, 1990
21*1990
Prediction of contact residue pairs based on co-substitution between sites in protein structures
S Miyazawa
PloS one 8 (1), e54252, 2013
182013
Selective constraints on amino acids estimated by a mechanistic codon substitution model with multiple nucleotide changes
S Miyazawa
PLoS One 6 (3), e17244, 2011
172011
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